June E. Pais, Ph.D.

Affiliations: 
2007 University of Michigan, Ann Arbor, Ann Arbor, MI 
Area:
Enzymology, metalloenzymes, ribozyme, RNA
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"June Pais"
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Carol A. Fierke grad student 2007 University of Michigan
 (Mechanism of catalysis and inhibition of mammalian protein farnesyltransferase.)
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Publications

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Hashimoto H, Pais JE, Dai N, et al. (2015) Structure of Naegleria Tet-like dioxygenase (NgTet1) in complexes with a reaction intermediate 5-hydroxymethylcytosine DNA. Nucleic Acids Research
Pais JE, Dai N, Tamanaha E, et al. (2015) Biochemical characterization of a Naegleria TET-like oxygenase and its application in single molecule sequencing of 5-methylcytosine. Proceedings of the National Academy of Sciences of the United States of America. 112: 4316-21
Hashimoto H, Pais JE, Zhang X, et al. (2014) Structure of a Naegleria Tet-like dioxygenase in complex with 5-methylcytosine DNA. Nature. 506: 391-5
Subramanian T, Pais JE, Liu S, et al. (2012) Farnesyl diphosphate analogues with aryl moieties are efficient alternate substrates for protein farnesyltransferase. Biochemistry. 51: 8307-19
Pais JE, Schilke B, Craig EA. (2011) Reevaluation of the role of the Pam18:Pam16 interaction in translocation of proteins by the mitochondrial Hsp70-based import motor. Molecular Biology of the Cell. 22: 4740-9
Krzysiak AJ, Rawat DS, Scott SA, et al. (2007) Combinatorial modulation of protein prenylation. Acs Chemical Biology. 2: 385-9
Pais JE, Fierke CA. (2007) Measurement of kinetic isotope effects to probe the reaction mechanism catalyzed by mammalian protein farnesyltransferase The Faseb Journal. 21
Pais JE, Bowers KE, Fierke CA. (2006) Measurement of the alpha-secondary kinetic isotope effect for the reaction catalyzed by mammalian protein farnesyltransferase. Journal of the American Chemical Society. 128: 15086-7
Pais JE, Bowers KE, Stoddard AK, et al. (2005) A continuous fluorescent assay for protein prenyltransferases measuring diphosphate release. Analytical Biochemistry. 345: 302-11
Karsten WE, Pais JE, Rao GS, et al. (2003) Ascaris suum NAD-malic enzyme is activated by L-malate and fumarate binding to separate allosteric sites. Biochemistry. 42: 9712-21
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